Nature Structural Biology
3, 671 - 675 (1996)
doi:10.1038/nsb0896-671
Structure of astacin with a transition-state analogue inhibitorFrank Grams1, 5, Vincent Dive2, Athanasios Yiotakis3, Irene Yiallouros4, Stamatia Vassiliou3, Robert Zwilling4, Wolfram Bode1
& Walter Stöcker4
1Max-Planck-lnstitut für Biochemie, Abt. Strukturforschung, Am Klopferspitz 18a, D-82152 Planegg-Martinsried, Germany
2CEA, Departement d'Ingenierie et d'Etudes des Proteines, C.E. Saclay, 91191 Gif Sur Yvette Cedex, France
3Department of Organic Chemistry, University of Athens, Panepistimiopolis, Zogratu, Athens 15771, Greece
4Zoologisches Institut der Universität Heidelberg, Physiologie, Im Neuenheimer Feld 230, D-69120 Heidelberg, Germany
5Present address: Boehringer Mannheim GmbH, Sandhofer Str. 116, Chemical Research, D-68305 Mannheim, Germany The structure of the zinc peptidase astacin in complex with a phosphinic peptide suggests that a special role is played by the side chain of a zinc-bound tyrosine, which is shifted to form a hydrogen bond to the phosphinyl group—a mimic of the carboxyanion of the transition state.
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